Cu-ZSM-5: A biomimetic inorganic model for methane oxidation
The present work highlights recent advances in elucidating the methane oxidation mechanism of the inorganic Cu-ZSM-5 biomimic and in identifying the reactive intermediates that are involved. Such understanding is important in view of upgrading abundantly available methane, but also to comprehend the...
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| Veröffentlicht in: | Journal of catalysis 2011-12, Vol.284 (2), p.157-164 |
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| container_title | Journal of catalysis |
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| creator | Vanelderen, Pieter Hadt, Ryan G. Smeets, Pieter J. Solomon, Edward I. Schoonheydt, Robert A. Sels, Bert F. |
| description | The present work highlights recent advances in elucidating the methane oxidation mechanism of the inorganic Cu-ZSM-5 biomimic and in identifying the reactive intermediates that are involved. Such understanding is important in view of upgrading abundantly available methane, but also to comprehend the working mechanism of genuine Cu-containing oxidation enzymes.
[Display omitted]
► Cu-ZSM-5 selectively oxidizes methane to methanol. ► The active site is a mono-μ-oxo bridged dicopper core. ► Dioxygen activation involves a
μ-(
η
2:
η
2) peroxo dicopper(II) species. ► While approaching the transition state of the reaction, the active site polarizes to a Cu
II-oxyl. ► The findings contribute to elucidating the working mechanism of methane-oxidizing Cu-enzymes.
The present work highlights recent advances in elucidating the methane oxidation mechanism of the inorganic Cu-ZSM-5 biomimic and in identifying the reactive intermediates that are involved. Such molecular understanding is important in view of upgrading abundantly available methane, but also to comprehend the working mechanism of genuine Cu-containing oxidation enzymes. |
| doi_str_mv | 10.1016/j.jcat.2011.10.009 |
| format | Article |
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[Display omitted]
► Cu-ZSM-5 selectively oxidizes methane to methanol. ► The active site is a mono-μ-oxo bridged dicopper core. ► Dioxygen activation involves a
μ-(
η
2:
η
2) peroxo dicopper(II) species. ► While approaching the transition state of the reaction, the active site polarizes to a Cu
II-oxyl. ► The findings contribute to elucidating the working mechanism of methane-oxidizing Cu-enzymes.
The present work highlights recent advances in elucidating the methane oxidation mechanism of the inorganic Cu-ZSM-5 biomimic and in identifying the reactive intermediates that are involved. Such molecular understanding is important in view of upgrading abundantly available methane, but also to comprehend the working mechanism of genuine Cu-containing oxidation enzymes.</description><identifier>ISSN: 0021-9517</identifier><identifier>EISSN: 1090-2694</identifier><identifier>DOI: 10.1016/j.jcat.2011.10.009</identifier><identifier>PMID: 23487537</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Bio-inorganic mimicking ; Biomimetics ; Cu-ZSM-5 ; C–H activation ; Dicopper(II)-oxo ; Dioxygen activation ; enzymes ; Inorganic chemistry ; Methane ; Oxidation ; Selective methane oxidation ; Zeolite</subject><ispartof>Journal of catalysis, 2011-12, Vol.284 (2), p.157-164</ispartof><rights>2011 Elsevier Inc.</rights><rights>Copyright © 2011 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c605t-d503b36b9c85af66b1f9a00358769215c2d24c1388d23958e13a897467c1648e3</citedby><cites>FETCH-LOGICAL-c605t-d503b36b9c85af66b1f9a00358769215c2d24c1388d23958e13a897467c1648e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0021951711003435$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23487537$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vanelderen, Pieter</creatorcontrib><creatorcontrib>Hadt, Ryan G.</creatorcontrib><creatorcontrib>Smeets, Pieter J.</creatorcontrib><creatorcontrib>Solomon, Edward I.</creatorcontrib><creatorcontrib>Schoonheydt, Robert A.</creatorcontrib><creatorcontrib>Sels, Bert F.</creatorcontrib><title>Cu-ZSM-5: A biomimetic inorganic model for methane oxidation</title><title>Journal of catalysis</title><addtitle>J Catal</addtitle><description>The present work highlights recent advances in elucidating the methane oxidation mechanism of the inorganic Cu-ZSM-5 biomimic and in identifying the reactive intermediates that are involved. Such understanding is important in view of upgrading abundantly available methane, but also to comprehend the working mechanism of genuine Cu-containing oxidation enzymes.
[Display omitted]
► Cu-ZSM-5 selectively oxidizes methane to methanol. ► The active site is a mono-μ-oxo bridged dicopper core. ► Dioxygen activation involves a
μ-(
η
2:
η
2) peroxo dicopper(II) species. ► While approaching the transition state of the reaction, the active site polarizes to a Cu
II-oxyl. ► The findings contribute to elucidating the working mechanism of methane-oxidizing Cu-enzymes.
The present work highlights recent advances in elucidating the methane oxidation mechanism of the inorganic Cu-ZSM-5 biomimic and in identifying the reactive intermediates that are involved. Such molecular understanding is important in view of upgrading abundantly available methane, but also to comprehend the working mechanism of genuine Cu-containing oxidation enzymes.</description><subject>Bio-inorganic mimicking</subject><subject>Biomimetics</subject><subject>Cu-ZSM-5</subject><subject>C–H activation</subject><subject>Dicopper(II)-oxo</subject><subject>Dioxygen activation</subject><subject>enzymes</subject><subject>Inorganic chemistry</subject><subject>Methane</subject><subject>Oxidation</subject><subject>Selective methane oxidation</subject><subject>Zeolite</subject><issn>0021-9517</issn><issn>1090-2694</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNqFkU1P3DAQhq2Kqmwpf6CHEvXEJcvYjr8QqoRW_ZJAPVAuXCzHcRZHSUztBJV_X0dLUdsD9cXWzDOvZ-ZF6C2GNQbMT7p1Z820JoBxDqwB1Au0wqCgJFxVe2gFQHCpGBb76HVKHWSQMfkK7RNaScGoWKGzzVzeXF2W7LQ4L2ofBj-4ydvCjyFuzZhfQ2hcX7QhFjlza0ZXhJ--MZMP4xv0sjV9coeP9wG6_vTx--ZLefHt89fN-UVpObCpbBjQmvJaWclMy3mNW2UAKJOCK4KZJQ2pLKZSNoQqJh2mRipRcWExr6SjB-jDTvdurgfXWDdO0fT6LvrBxAcdjNd_Z0Z_q7fhXlOmqKp4Fjh-FIjhx-zSpAefrOv7PE6YkyaQDxb5s_-iWNK8QyZgUX3_D9qFOY55E1qBgIpitUBkB9kYUoqufWobg15s1J1ebNSLjUss25iL3v058FPJb98ycLQDWhO02Uaf9PVVVuDLHBVnyxxnO8JlY-69izpZ70brGh-dnXQT_HMd_AIW1LRP</recordid><startdate>20111201</startdate><enddate>20111201</enddate><creator>Vanelderen, Pieter</creator><creator>Hadt, Ryan G.</creator><creator>Smeets, Pieter J.</creator><creator>Solomon, Edward I.</creator><creator>Schoonheydt, Robert A.</creator><creator>Sels, Bert F.</creator><general>Elsevier Inc</general><general>Elsevier BV</general><scope>FBQ</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20111201</creationdate><title>Cu-ZSM-5: A biomimetic inorganic model for methane oxidation</title><author>Vanelderen, Pieter ; Hadt, Ryan G. ; Smeets, Pieter J. ; Solomon, Edward I. ; Schoonheydt, Robert A. ; Sels, Bert F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c605t-d503b36b9c85af66b1f9a00358769215c2d24c1388d23958e13a897467c1648e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Bio-inorganic mimicking</topic><topic>Biomimetics</topic><topic>Cu-ZSM-5</topic><topic>C–H activation</topic><topic>Dicopper(II)-oxo</topic><topic>Dioxygen activation</topic><topic>enzymes</topic><topic>Inorganic chemistry</topic><topic>Methane</topic><topic>Oxidation</topic><topic>Selective methane oxidation</topic><topic>Zeolite</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vanelderen, Pieter</creatorcontrib><creatorcontrib>Hadt, Ryan G.</creatorcontrib><creatorcontrib>Smeets, Pieter J.</creatorcontrib><creatorcontrib>Solomon, Edward I.</creatorcontrib><creatorcontrib>Schoonheydt, Robert A.</creatorcontrib><creatorcontrib>Sels, Bert F.</creatorcontrib><collection>AGRIS</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of catalysis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vanelderen, Pieter</au><au>Hadt, Ryan G.</au><au>Smeets, Pieter J.</au><au>Solomon, Edward I.</au><au>Schoonheydt, Robert A.</au><au>Sels, Bert F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cu-ZSM-5: A biomimetic inorganic model for methane oxidation</atitle><jtitle>Journal of catalysis</jtitle><addtitle>J Catal</addtitle><date>2011-12-01</date><risdate>2011</risdate><volume>284</volume><issue>2</issue><spage>157</spage><epage>164</epage><pages>157-164</pages><issn>0021-9517</issn><eissn>1090-2694</eissn><abstract>The present work highlights recent advances in elucidating the methane oxidation mechanism of the inorganic Cu-ZSM-5 biomimic and in identifying the reactive intermediates that are involved. Such understanding is important in view of upgrading abundantly available methane, but also to comprehend the working mechanism of genuine Cu-containing oxidation enzymes.
[Display omitted]
► Cu-ZSM-5 selectively oxidizes methane to methanol. ► The active site is a mono-μ-oxo bridged dicopper core. ► Dioxygen activation involves a
μ-(
η
2:
η
2) peroxo dicopper(II) species. ► While approaching the transition state of the reaction, the active site polarizes to a Cu
II-oxyl. ► The findings contribute to elucidating the working mechanism of methane-oxidizing Cu-enzymes.
The present work highlights recent advances in elucidating the methane oxidation mechanism of the inorganic Cu-ZSM-5 biomimic and in identifying the reactive intermediates that are involved. Such molecular understanding is important in view of upgrading abundantly available methane, but also to comprehend the working mechanism of genuine Cu-containing oxidation enzymes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>23487537</pmid><doi>10.1016/j.jcat.2011.10.009</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | Elsevier ScienceDirect Journals |
| subjects | Bio-inorganic mimicking Biomimetics Cu-ZSM-5 C–H activation Dicopper(II)-oxo Dioxygen activation enzymes Inorganic chemistry Methane Oxidation Selective methane oxidation Zeolite |
| title | Cu-ZSM-5: A biomimetic inorganic model for methane oxidation |
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